ID ZYX_HUMAN Reviewed; 572 AA. AC Q15942; A4D2G6; B4DQX7; Q6I9S4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 215. DE RecName: Full=Zyxin; DE AltName: Full=Zyxin-2; GN Name=ZYX; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Umbilical vein; RX PubMed=8940160; DOI=10.1074/jbc.271.49.31470; RA Macalma T., Otte J., Hensler M.E., Bockholt S.M., Louis H.A., RA Kalff-Suske M., Grzeschik K.H., von der Ahe D., Beckerle M.C.; RT "Molecular characterization of human zyxin."; RL J. Biol. Chem. 271:31470-31478(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=8917469; DOI=10.1111/j.1432-1033.1996.00657.x; RA Zumbrunn J., Trueb B.; RT "A zyxin-related protein whose synthesis is reduced in virally transformed RT fibroblasts."; RL Eur. J. Biochem. 241:657-663(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney, Skin, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 2-25; 36-54; 168-184; 280-320 AND 325-375, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Calvo F.; RL Submitted (FEB-2008) to UniProtKB. RN [10] RP INTERACTION WITH ENAH AND VASP, AND MUTAGENESIS OF PHE-71; PHE-93; PHE-104 RP AND PHE-114. RX PubMed=10801818; DOI=10.1074/jbc.m001698200; RA Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C., RA Golsteyn R.M.; RT "Characterization of the interaction between zyxin and members of the RT Ena/vasodilator-stimulated phosphoprotein family of proteins."; RL J. Biol. Chem. 275:22503-22511(2000). RN [11] RP INTERACTION WITH HPV6 E6 (MICROBIAL INFECTION). RX PubMed=11689660; DOI=10.1128/jvi.75.23.11791-11802.2001; RA Degenhardt Y.Y., Silverstein S.; RT "Interaction of zyxin, a focal adhesion protein, with the E6 protein from RT human papillomavirus type 6 results in its nuclear translocation."; RL J. Virol. 75:11791-11802(2001). RN [12] RP SUBCELLULAR LOCATION, AND INTERACTION WITH TES. RX PubMed=12695497; DOI=10.1083/jcb.200211015; RA Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N., RA Koecher T., Piddini E., Griffiths G., Way M.; RT "The conformational state of Tes regulates its zyxin-dependent recruitment RT to focal adhesions."; RL J. Cell Biol. 161:33-39(2003). RN [13] RP INTERACTION WITH SYNPO2. RX PubMed=16885336; DOI=10.1158/0008-5472.can-06-0227; RA Yu Y.P., Luo J.H.; RT "Myopodin-mediated suppression of prostate cancer cell migration involves RT interaction with zyxin."; RL Cancer Res. 66:7414-7419(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-281, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [17] RP INTERACTION WITH EVL; VASP AND ENAH. RX PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033; RA Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J., RA McDonald N.Q., Way M.; RT "Tes, a specific Mena interacting partner, breaks the rules for EVH1 RT binding."; RL Mol. Cell 28:1071-1082(2007). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=18297730; DOI=10.1002/dvdy.21471; RA Martynova N.Y., Eroshkin F.M., Ermolina L.V., Ermakova G.V., RA Korotaeva A.L., Smurova K.M., Gyoeva F.K., Zaraisky A.G.; RT "The LIM-domain protein zyxin binds the homeodomain factor Xanf1/Hesx1 and RT modulates its activity in the anterior neural plate of Xenopus laevis RT embryo."; RL Dev. Dyn. 237:736-749(2008). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; SER-281 AND SER-344, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-259; SER-267; RP THR-270; THR-274; SER-281; SER-288; SER-308 AND SER-344, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-179; SER-259; RP THR-274; SER-281; SER-308 AND SER-344, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; THR-270; SER-281 AND RP SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-170; SER-259; RP SER-267; THR-270; SER-281; SER-308 AND SER-344, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-142; SER-259; RP SER-267; SER-281 AND SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [32] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP CC protein. Important for targeting TES and ENA/VASP family members to CC focal adhesions and for the formation of actin-rich structures. May be CC a component of a signal transduction pathway that mediates adhesion- CC stimulated changes in gene expression (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with HPV type 6 protein E6. Does not interact CC significantly with E6 proteins from HPV types 11, 16, or 18. Interacts, CC via the Pro-rich regions, with the EVH1 domains of ENAH, EVL and VASP. CC Interacts with the first LIM domain of TES. Interacts with NEBL CC (isoform 2). Interacts with SYNPO2. {ECO:0000269|PubMed:10801818, CC ECO:0000269|PubMed:12695497, ECO:0000269|PubMed:16885336, CC ECO:0000269|PubMed:18158903}. CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus type CC 6/HPV6 protein E6. Does not interact significantly with E6 proteins CC from HPV types 11, 16, or 18. {ECO:0000269|PubMed:11689660}. CC -!- INTERACTION: CC Q15942; Q9NQ75-2: CASS4; NbExp=4; IntAct=EBI-444225, EBI-12270182; CC Q15942; Q9UI08-2: EVL; NbExp=5; IntAct=EBI-444225, EBI-6448852; CC Q15942; Q9NV31: IMP3; NbExp=8; IntAct=EBI-444225, EBI-747481; CC Q15942; P28838: LAP3; NbExp=3; IntAct=EBI-444225, EBI-2339312; CC Q15942; O95835: LATS1; NbExp=10; IntAct=EBI-444225, EBI-444209; CC Q15942; O14910: LIN7A; NbExp=3; IntAct=EBI-444225, EBI-2513988; CC Q15942; A0A0S2Z4M0: NME5; NbExp=4; IntAct=EBI-444225, EBI-16430544; CC Q15942; P35372: OPRM1; NbExp=2; IntAct=EBI-444225, EBI-2624570; CC Q15942; Q96HC4: PDLIM5; NbExp=3; IntAct=EBI-444225, EBI-751267; CC Q15942; Q96BD5: PHF21A; NbExp=6; IntAct=EBI-444225, EBI-745085; CC Q15942; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-444225, EBI-2798044; CC Q15942; Q8WWV3: RTN4IP1; NbExp=5; IntAct=EBI-444225, EBI-743502; CC Q15942; P50552: VASP; NbExp=4; IntAct=EBI-444225, EBI-748201; CC Q15942; Q96KM6: ZNF512B; NbExp=3; IntAct=EBI-444225, EBI-1049952; CC Q15942; B2R9Y1; NbExp=3; IntAct=EBI-444225, EBI-10175746; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Cell CC junction, focal adhesion. Note=Associates with the actin cytoskeleton CC near the adhesion plaques. Enters the nucleus in the presence of HESX1. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15942-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15942-2; Sequence=VSP_057288; CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X94991; CAA64447.1; -; mRNA. DR EMBL; X95735; CAA65050.1; -; mRNA. DR EMBL; AK299005; BAG61089.1; -; mRNA. DR EMBL; AK316227; BAH14598.1; -; mRNA. DR EMBL; CR457431; CAG33712.1; -; mRNA. DR EMBL; AC092214; AAS07459.1; -; Genomic_DNA. DR EMBL; CH236959; EAL23788.1; -; Genomic_DNA. DR EMBL; CH471198; EAW51848.1; -; Genomic_DNA. DR EMBL; BC008743; AAH08743.1; -; mRNA. DR EMBL; BC009360; AAH09360.1; -; mRNA. DR EMBL; BC010031; AAH10031.1; -; mRNA. DR CCDS; CCDS5883.1; -. [Q15942-1] DR PIR; G02845; G02845. DR RefSeq; NP_001010972.1; NM_001010972.1. [Q15942-1] DR RefSeq; NP_003452.1; NM_003461.4. [Q15942-1] DR AlphaFoldDB; Q15942; -. DR SMR; Q15942; -. DR BioGRID; 113569; 316. DR CORUM; Q15942; -. DR IntAct; Q15942; 97. DR MINT; Q15942; -. DR STRING; 9606.ENSP00000324422; -. DR ChEMBL; CHEMBL4295832; -. DR DrugBank; DB11638; Artenimol. DR GlyCosmos; Q15942; 18 sites, 3 glycans. DR GlyGen; Q15942; 24 sites, 3 O-linked glycans (24 sites). DR iPTMnet; Q15942; -. DR MetOSite; Q15942; -. DR PhosphoSitePlus; Q15942; -. DR SwissPalm; Q15942; -. DR BioMuta; ZYX; -. DR DMDM; 2497677; -. DR OGP; Q15942; -. DR CPTAC; CPTAC-1022; -. DR CPTAC; CPTAC-452; -. DR CPTAC; CPTAC-453; -. DR EPD; Q15942; -. DR jPOST; Q15942; -. DR MassIVE; Q15942; -. DR MaxQB; Q15942; -. DR PaxDb; 9606-ENSP00000324422; -. DR PeptideAtlas; Q15942; -. DR ProteomicsDB; 4911; -. DR ProteomicsDB; 60823; -. [Q15942-1] DR Pumba; Q15942; -. DR Antibodypedia; 1394; 449 antibodies from 43 providers. DR DNASU; 7791; -. DR Ensembl; ENST00000322764.10; ENSP00000324422.5; ENSG00000159840.16. [Q15942-1] DR Ensembl; ENST00000392910.6; ENSP00000376642.2; ENSG00000159840.16. [Q15942-2] DR Ensembl; ENST00000645637.1; ENSP00000495629.1; ENSG00000285443.2. [Q15942-2] DR Ensembl; ENST00000646695.2; ENSP00000494798.1; ENSG00000285443.2. [Q15942-1] DR GeneID; 7791; -. DR KEGG; hsa:7791; -. DR MANE-Select; ENST00000322764.10; ENSP00000324422.5; NM_003461.5; NP_003452.1. DR UCSC; uc003wcx.5; human. [Q15942-1] DR AGR; HGNC:13200; -. DR CTD; 7791; -. DR DisGeNET; 7791; -. DR GeneCards; ZYX; -. DR HGNC; HGNC:13200; ZYX. DR HPA; ENSG00000159840; Low tissue specificity. DR MIM; 602002; gene. DR neXtProt; NX_Q15942; -. DR OpenTargets; ENSG00000159840; -. DR PharmGKB; PA37765; -. DR VEuPathDB; HostDB:ENSG00000159840; -. DR eggNOG; KOG1701; Eukaryota. DR GeneTree; ENSGT00940000154273; -. DR HOGENOM; CLU_001357_10_2_1; -. DR InParanoid; Q15942; -. DR OMA; YAPKCSV; -. DR OrthoDB; 370973at2759; -. DR PhylomeDB; Q15942; -. DR TreeFam; TF320310; -. DR PathwayCommons; Q15942; -. DR SignaLink; Q15942; -. DR SIGNOR; Q15942; -. DR BioGRID-ORCS; 7791; 24 hits in 1161 CRISPR screens. DR ChiTaRS; ZYX; human. DR GeneWiki; Zyxin; -. DR GenomeRNAi; 7791; -. DR Pharos; Q15942; Tbio. DR PRO; PR:Q15942; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q15942; Protein. DR Bgee; ENSG00000159840; Expressed in body of uterus and 98 other cell types or tissues. DR ExpressionAtlas; Q15942; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005912; C:adherens junction; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0007160; P:cell-matrix adhesion; IC:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB. DR CDD; cd09349; LIM1_Zyxin; 1. DR CDD; cd09435; LIM3_Zyxin; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 3. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24212:SF1; ZYXIN; 1. DR PANTHER; PTHR24212; ZYXIN/TRIP6; 1. DR Pfam; PF00412; LIM; 3. DR SMART; SM00132; LIM; 3. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2. DR PROSITE; PS00478; LIM_DOMAIN_1; 2. DR PROSITE; PS50023; LIM_DOMAIN_2; 3. DR Genevisible; Q15942; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell adhesion; Cell junction; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Host-virus interaction; KW LIM domain; Metal-binding; Methylation; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330" FT CHAIN 2..572 FT /note="Zyxin" FT /id="PRO_0000075913" FT DOMAIN 384..443 FT /note="LIM zinc-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 444..503 FT /note="LIM zinc-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 504..570 FT /note="LIM zinc-binding 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT REGION 23..351 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 61..79 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 91..139 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 211..254 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 255..269 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 306..320 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 332..346 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330" FT MOD_RES 116 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62523" FT MOD_RES 169 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 179 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 253 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q62523" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 265 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q62523" FT MOD_RES 267 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 270 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 272 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q62523" FT MOD_RES 274 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 279 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 281 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 288 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 308 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..157 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057288" FT VARIANT 223 FT /note="H -> L (in dbSNP:rs11978404)" FT /id="VAR_034081" FT MUTAGEN 71 FT /note="F->A: Reduced interaction with ENAH and VASP." FT /evidence="ECO:0000269|PubMed:10801818" FT MUTAGEN 93 FT /note="F->A: Reduced interaction with ENAH and VASP." FT /evidence="ECO:0000269|PubMed:10801818" FT MUTAGEN 104 FT /note="F->A: Greatly reduced interaction with ENAH and FT VASP; when associated with A-71 or with A-71 and A-93." FT /evidence="ECO:0000269|PubMed:10801818" FT MUTAGEN 114 FT /note="F->A: No targeting to focal adhesions and reduced FT actin-rich structures; when associated with A-71; A-93 and FT A-104." FT /evidence="ECO:0000269|PubMed:10801818" SQ SEQUENCE 572 AA; 61277 MW; 2833B1EFA260B762 CRC64; MAAPRPSPAI SVSVSAPAFY APQKKFGPVV APKPKVNPFR PGDSEPPPAP GAQRAQMGRV GEIPPPPPED FPLPPPPLAG DGDDAEGALG GAFPPPPPPI EESFPPAPLE EEIFPSPPPP PEEEGGPEAP IPPPPQPREK VSSIDLEIDS LSSLLDDMTK NDPFKARVSS GYVPPPVATP FSSKSSTKPA AGGTAPLPPW KSPSSSQPLP QVPAPAQSQT QFHVQPQPQP KPQVQLHVQS QTQPVSLANT QPRGPPASSP APAPKFSPVT PKFTPVASKF SPGAPGGSGS QPNQKLGHPE ALSAGTGSPQ PPSFTYAQQR EKPRVQEKQH PVPPPAQNQN QVRSPGAPGP LTLKEVEELE QLTQQLMQDM EHPQRQNVAV NELCGRCHQP LARAQPAVRA LGQLFHIACF TCHQCAQQLQ GQQFYSLEGA PYCEGCYTDT LEKCNTCGEP ITDRMLRATG KAYHPHCFTC VVCARPLEGT SFIVDQANRP HCVPDYHKQY APRCSVCSEP IMPEPGRDET VRVVALDKNF HMKCYKCEDC GKPLSIEADD NGCFPLDGHV LCRKCHTARA QT //